PATL1_ARATH - dbPTM
PATL1_ARATH - PTM Information in dbPTM
Basic Information of Protein
UniProt ID PATL1_ARATH
UniProt AC Q56WK6
Protein Name Patellin-1
Gene Name PATL1
Organism Arabidopsis thaliana (Mouse-ear cress).
Sequence Length 573
Subcellular Localization Membrane . Cytoplasm . Mainly membrane-associated. Also cytoplasmic. Cell plate during cell division.
Protein Description Carrier protein that may be involved in membrane-trafficking events associated with cell plate formation during cytokinesis. Binds to some hydrophobic molecules and promotes their transfer between the different cellular sites. Binds to phosphoinositides with a preference for PtdIns(5)P, PtdIns(4,5)P2 and PtdIns(3)P..
Protein Sequence MAQEEVQKSADVAAAPVVKEKPITDKEVTIPTPVAEKEEVAAPVSDEKAVPEKEVTPEKEAPAAEAEKSVSVKEEETVVVAEKVVVLTAEEVQKKALEEFKELVREALNKREFTAPVTPVKEEKTEEKKTEEETKEEEKTEEKKEETTTEVKVEEEKPAVPAAEEEKSSEAAPVETKSEEKPEEKAEVTTEKASSAEEDGTKTVEAIEESIVSVSPPESAVAPVVVETVAVAEAEPVEPEEVSIWGVPLLQDERSDVILTKFLRARDFKVKEALTMLKNTVQWRKENKIDELVESGEEVSEFEKMVFAHGVDKEGHVVIYSSYGEFQNKELFSDKEKLNKFLSWRIQLQEKCVRAIDFSNPEAKSSFVFVSDFRNAPGLGKRALWQFIRRAVKQFEDNYPEFAAKELFINVPWWYIPYYKTFGSIITSPRTRSKMVLAGPSKSADTIFKYIAPEQVPVKYGGLSKDTPLTEETITEAIVKPAANYTIELPASEACTLSWELRVLGADVSYGAQFEPTTEGSYAVIVSKTRKIGSTDEPVITDSFKVGEPGKIVITIDNQTSKKKKVLYRFKTQ
Overview of Protein Modification Sites with Functional and Structural Information
Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations Modification Substrate Peptides
&
Secondary Structure		 ASA (%) Reference Orthologous
Protein Cluster
2Acetylation------MAQEEVQKS
------CCHHHHHHH		26.0322223895
9PhosphorylationAQEEVQKSADVAAAP
CHHHHHHHHCCCCCC		16.7725561503
24PhosphorylationVVKEKPITDKEVTIP
EECCCCCCCCEEECC		49.9323776212
29PhosphorylationPITDKEVTIPTPVAE
CCCCCEEECCCCCCC		23.4823776212
32PhosphorylationDKEVTIPTPVAEKEE
CCEEECCCCCCCCCE		26.9223776212
45PhosphorylationEEVAAPVSDEKAVPE
CEEECCCCCCCCCCC		38.7130291188
56PhosphorylationAVPEKEVTPEKEAPA
CCCCCCCCCCCCCCH		27.1617317660
69PhosphorylationPAAEAEKSVSVKEEE
CHHHHHHCCCCCCCC		15.8924601666
71PhosphorylationAEAEKSVSVKEEETV
HHHHHCCCCCCCCEE		34.2630291188
77PhosphorylationVSVKEEETVVVAEKV
CCCCCCCEEEEEEEE		23.1419376835
114PhosphorylationALNKREFTAPVTPVK
HHHCCCCCCCCCCCC		25.8719376835
118PhosphorylationREFTAPVTPVKEEKT
CCCCCCCCCCCCHHC		22.7030291188
140PhosphorylationETKEEEKTEEKKEET
HHHHHHHHHHHHHCC		53.2919880383
168PhosphorylationPAAEEEKSSEAAPVE
CHHHHHHCCCCCCCC		36.3723776212
169PhosphorylationAAEEEKSSEAAPVET
HHHHHHCCCCCCCCC		42.1823776212
176PhosphorylationSEAAPVETKSEEKPE
CCCCCCCCCCCCCHH		39.8523776212
178PhosphorylationAAPVETKSEEKPEEK
CCCCCCCCCCCHHHH		59.4130291188
189PhosphorylationPEEKAEVTTEKASSA
HHHHHCCCCHHHCCC		22.2723776212
190PhosphorylationEEKAEVTTEKASSAE
HHHHCCCCHHHCCCC		40.4423776212
194PhosphorylationEVTTEKASSAEEDGT
CCCCHHHCCCCCCCC		40.9423776212
195PhosphorylationVTTEKASSAEEDGTK
CCCHHHCCCCCCCCC		44.5523776212
201PhosphorylationSSAEEDGTKTVEAIE
CCCCCCCCCHHHHHH		35.5423776212
285UbiquitinationKNTVQWRKENKIDEL
HHHHHHHHHCCHHHH		63.7819292762
305SulfoxidationEVSEFEKMVFAHGVD
CHHHHHHHHHHCCCC		2.0625693801
366PhosphorylationSNPEAKSSFVFVSDF
CCHHHHCCEEEEECC		25.4029654922
424PhosphorylationPYYKTFGSIITSPRT
CHHHHHHHHCCCCCC		13.4623776212
427PhosphorylationKTFGSIITSPRTRSK
HHHHHHCCCCCCCCC		30.8923776212
428PhosphorylationTFGSIITSPRTRSKM
HHHHHCCCCCCCCCE		11.2830291188
433PhosphorylationITSPRTRSKMVLAGP
CCCCCCCCCEEEECC		25.2119880383
441PhosphorylationKMVLAGPSKSADTIF
CEEEECCCCCCCHHH		38.0219880383
443PhosphorylationVLAGPSKSADTIFKY
EEECCCCCCCHHHHH		35.4019880383
446PhosphorylationGPSKSADTIFKYIAP
CCCCCCCHHHHHHCC		28.2019880383
Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)
Modified Location Modified Residue Modification Type of Upstream Proteins Gene Name of Upstream Proteins UniProt AC of Upstream Proteins Sources

Oops, there are no upstream regulatory protein records of PATL1_ARATH !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of PATL1_ARATH !!
Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Modified Location Modification Variant Position
(Distance <= 10) 		Residue Change SAP Related Disease Reference

Oops, there are no SNP-PTM records of PATL1_ARATH !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of PATL1_ARATH

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Large-scale Arabidopsis phosphoproteome profiling reveals novelchloroplast kinase substrates and phosphorylation networks.";
Reiland S., Messerli G., Baerenfaller K., Gerrits B., Endler A.,Grossmann J., Gruissem W., Baginsky S.;
Plant Physiol. 150:889-903(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-32; SER-45; THR-56;THR-118 AND SER-194, AND MASS SPECTROMETRY.
Ubiquitylation
ReferencePubMed
"Tandem affinity purification and mass spectrometric analysis ofubiquitylated proteins in Arabidopsis.";
Saracco S.A., Hansson M., Scalf M., Walker J.M., Smith L.M.,Vierstra R.D.;
Plant J. 59:344-358(2009).
Cited for: UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-285, AND IDENTIFICATIONBY MASS SPECTROMETRY.

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